ACBP_HUMAN
ID ACBP_HUMAN Reviewed; 87 AA.
AC P07108; B8ZWD2; B8ZWD6; B8ZWD7; P08869; Q4VWZ6; Q53SQ7; Q6IB48; Q9UCI8;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Acyl-CoA-binding protein;
DE Short=ACBP;
DE AltName: Full=Diazepam-binding inhibitor;
DE Short=DBI;
DE AltName: Full=Endozepine;
DE Short=EP;
GN Name=DBI;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3020548; DOI=10.1073/pnas.83.19.7547;
RA Gray P.W., Glaister D., Seeburg P.H., Guidotti A., Costa E.;
RT "Cloning and expression of cDNA for human diazepam binding inhibitor, a
RT natural ligand of an allosteric regulatory site of the gamma-aminobutyric
RT acid type A receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:7547-7551(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2881742; DOI=10.1089/dna.1987.6.71;
RA Webb N.R., Rose T.M., Malik N., Marquardt H., Shoyab M., Todaro G.J.,
RA Lee D.C.;
RT "Bovine and human cDNA sequences encoding a putative benzodiazepine
RT receptor ligand.";
RL DNA 6:71-79(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=16055366; DOI=10.1016/j.biocel.2005.06.008;
RA Nitz I., Doering F., Schrezenmeir J., Burwinkel B.;
RT "Identification of new acyl-CoA binding protein transcripts in human and
RT mouse.";
RL Int. J. Biochem. Cell Biol. 37:2395-2405(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=21698759; DOI=10.1002/iub.471;
RA Ludewig A.H., Nitz I., Klapper M., Doring F.;
RT "Identification of a novel human Acyl-CoA binding protein isoform with a
RT unique C-terminal domain.";
RL IUBMB Life 63:547-552(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4 AND 5), ALTERNATIVE SPLICING, AND
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=20345851; DOI=10.1111/j.1582-4934.2010.01055.x;
RA Nitz I., Kruse M.L., Klapper M., Doring F.;
RT "Specific regulation of low-abundance transcript variants encoding human
RT Acyl-CoA binding protein (ACBP) isoforms.";
RL J. Cell. Mol. Med. 15:909-927(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PROTEIN SEQUENCE OF 2-87 (ISOFORM 1), AND ACETYLATION AT SER-2.
RC TISSUE=Brain;
RX PubMed=3525533; DOI=10.1016/s0021-9258(18)67575-1;
RA Marquardt H., Todaro G.J., Shoyab M.;
RT "Complete amino acid sequences of bovine and human endozepines. Homology
RT with rat diazepam binding inhibitor.";
RL J. Biol. Chem. 261:9727-9731(1986).
RN [11]
RP PROTEIN SEQUENCE OF 2-14 (ISOFORM 1).
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP PROTEIN SEQUENCE OF 26-30 AND 72-87.
RX PubMed=1292782; DOI=10.1097/00008390-199212000-00006;
RA Apfel R., Lottspeich F., Hoppe J., Behl C., Duerr G., Bogdahn U.;
RT "Purification and analysis of growth regulating proteins secreted by a
RT human melanoma cell line.";
RL Melanoma Res. 2:327-336(1992).
RN [13]
RP ALTERNATIVE SPLICING.
RX PubMed=7534063; DOI=10.1042/bj3060327;
RA Kolmer M., Rovio A., Alho H.;
RT "The characterization of two diazepam binding inhibitor (DBI) transcripts
RT in humans.";
RL Biochem. J. 306:327-330(1995).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=17953517; DOI=10.1042/bj20070559;
RA Hansen J.S., Faergeman N.J., Kragelund B.B., Knudsen J.;
RT "Acyl-CoA-binding protein (ACBP) localizes to the endoplasmic reticulum and
RT Golgi in a ligand-dependent manner in mammalian cells.";
RL Biochem. J. 410:463-472(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8; LYS-19; LYS-55 AND LYS-77, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP MALONYLATION AT LYS-55.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [23]
RP HYDROXYBUTYRYLATION AT LYS-55.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH ACYL-COENZYME A.
RX PubMed=17044054; DOI=10.1002/prot.21124;
RA Taskinen J.P., van Aalten D.M., Knudsen J., Wierenga R.K.;
RT "High resolution crystal structures of unliganded and liganded human liver
RT ACBP reveal a new mode of binding for the acyl-CoA ligand.";
RL Proteins 66:229-238(2007).
CC -!- FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high
CC affinity and may function as an intracellular carrier of acyl-CoA
CC esters. It is also able to displace diazepam from the benzodiazepine
CC (BZD) recognition site located on the GABA type A receptor. It is
CC therefore possible that this protein also acts as a neuropeptide to
CC modulate the action of the GABA receptor.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:17044054}.
CC -!- INTERACTION:
CC P07108-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12847580, EBI-742054;
CC P07108-2; Q9UHV9: PFDN2; NbExp=3; IntAct=EBI-12847580, EBI-359873;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Golgi
CC apparatus {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}.
CC Note=Golgi localization is dependent on ligand binding
CC (PubMed:17953517). {ECO:0000269|PubMed:17953517}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=ACBP-1a, Short;
CC IsoId=P07108-1; Sequence=Displayed;
CC Name=2; Synonyms=ACBP-1b, Long;
CC IsoId=P07108-2; Sequence=VSP_000068;
CC Name=3; Synonyms=ACBP-1c;
CC IsoId=P07108-3; Sequence=VSP_038680;
CC Name=4; Synonyms=ACBP-1a1-g;
CC IsoId=P07108-4; Sequence=VSP_043437;
CC Name=5; Synonyms=ACBP-1g;
CC IsoId=P07108-5; Sequence=VSP_043438;
CC Name=6; Synonyms=ACBP-1e;
CC IsoId=P07108-6; Sequence=VSP_044114;
CC -!- TISSUE SPECIFICITY: Isoform 1 is ubiquitous, with a moderate expression
CC level. Isoform 2 is ubiquitous with high level in liver and adipose
CC tissue. Isoform 3 is ubiquitous with strong expression in adipose
CC tissue and heart. {ECO:0000269|PubMed:16055366,
CC ECO:0000269|PubMed:21698759}.
CC -!- MISCELLANEOUS: [Isoform 6]: Predominantly expressed in adipose tissue
CC and hippocampus. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ACBP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M14200; AAA52171.1; -; mRNA.
DR EMBL; M15887; AAA35788.1; -; mRNA.
DR EMBL; FM213123; CAR82405.1; -; mRNA.
DR EMBL; FM213124; CAR82406.1; -; mRNA.
DR EMBL; FM213125; CAR82407.1; -; mRNA.
DR EMBL; FM213126; CAR82408.1; -; mRNA.
DR EMBL; FM213127; CAR82409.1; -; mRNA.
DR EMBL; FM213128; CAR82410.1; -; mRNA.
DR EMBL; FM213131; CAR82414.1; -; mRNA.
DR EMBL; CR456956; CAG33237.1; -; mRNA.
DR EMBL; AC016736; AAY14873.1; -; Genomic_DNA.
DR EMBL; CH471103; EAW95214.1; -; Genomic_DNA.
DR EMBL; BC006466; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC062996; AAH62996.1; -; mRNA.
DR EMBL; AM000001; CAJ00736.1; -; mRNA.
DR CCDS; CCDS2126.1; -. [P07108-2]
DR CCDS; CCDS42740.1; -. [P07108-1]
DR CCDS; CCDS42741.1; -. [P07108-3]
DR CCDS; CCDS54390.1; -. [P07108-4]
DR CCDS; CCDS54391.1; -. [P07108-5]
DR PIR; B26448; NZHU.
DR RefSeq; NP_001073331.1; NM_001079862.2. [P07108-1]
DR RefSeq; NP_001073332.1; NM_001079863.1. [P07108-3]
DR RefSeq; NP_001171488.1; NM_001178017.1. [P07108-5]
DR RefSeq; NP_001171512.1; NM_001178041.2. [P07108-4]
DR RefSeq; NP_001171513.1; NM_001178042.2. [P07108-2]
DR RefSeq; NP_001269562.1; NM_001282633.1. [P07108-2]
DR RefSeq; NP_001269563.1; NM_001282634.1. [P07108-2]
DR RefSeq; NP_001269564.1; NM_001282635.1. [P07108-2]
DR RefSeq; NP_065438.1; NM_020548.7. [P07108-2]
DR PDB; 2CB8; X-ray; 1.40 A; A/B=2-87.
DR PDB; 2FJ9; X-ray; 1.60 A; A=2-87.
DR PDBsum; 2CB8; -.
DR PDBsum; 2FJ9; -.
DR AlphaFoldDB; P07108; -.
DR SMR; P07108; -.
DR BioGRID; 107990; 30.
DR IntAct; P07108; 17.
DR MINT; P07108; -.
DR STRING; 9606.ENSP00000439012; -.
DR DrugBank; DB01992; Coenzyme A.
DR DrugBank; DB03381; Hexadecanal.
DR iPTMnet; P07108; -.
DR MetOSite; P07108; -.
DR PhosphoSitePlus; P07108; -.
DR SwissPalm; P07108; -.
DR BioMuta; DBI; -.
DR EPD; P07108; -.
DR jPOST; P07108; -.
DR MassIVE; P07108; -.
DR MaxQB; P07108; -.
DR PaxDb; P07108; -.
DR PeptideAtlas; P07108; -.
DR PRIDE; P07108; -.
DR ProteomicsDB; 51954; -. [P07108-1]
DR ProteomicsDB; 51955; -. [P07108-2]
DR ProteomicsDB; 51956; -. [P07108-3]
DR ProteomicsDB; 51957; -. [P07108-4]
DR ProteomicsDB; 51958; -. [P07108-5]
DR TopDownProteomics; P07108-1; -. [P07108-1]
DR TopDownProteomics; P07108-3; -. [P07108-3]
DR TopDownProteomics; P07108-4; -. [P07108-4]
DR TopDownProteomics; P07108-5; -. [P07108-5]
DR Antibodypedia; 33373; 369 antibodies from 32 providers.
DR DNASU; 1622; -.
DR Ensembl; ENST00000311521.8; ENSP00000311117.4; ENSG00000155368.18. [P07108-2]
DR Ensembl; ENST00000355857.8; ENSP00000348116.3; ENSG00000155368.18. [P07108-1]
DR Ensembl; ENST00000393103.2; ENSP00000376815.2; ENSG00000155368.18. [P07108-3]
DR Ensembl; ENST00000409094.5; ENSP00000386486.1; ENSG00000155368.18. [P07108-2]
DR Ensembl; ENST00000535757.5; ENSP00000439012.1; ENSG00000155368.18. [P07108-2]
DR Ensembl; ENST00000627093.2; ENSP00000486281.1; ENSG00000155368.18. [P07108-4]
DR Ensembl; ENST00000627305.2; ENSP00000486361.1; ENSG00000155368.18. [P07108-5]
DR GeneID; 1622; -.
DR KEGG; hsa:1622; -.
DR MANE-Select; ENST00000355857.8; ENSP00000348116.3; NM_001079862.4; NP_001073331.1.
DR UCSC; uc002tlv.5; human. [P07108-1]
DR CTD; 1622; -.
DR DisGeNET; 1622; -.
DR GeneCards; DBI; -.
DR HGNC; HGNC:2690; DBI.
DR HPA; ENSG00000155368; Low tissue specificity.
DR MIM; 125950; gene.
DR neXtProt; NX_P07108; -.
DR OpenTargets; ENSG00000155368; -.
DR PharmGKB; PA27158; -.
DR VEuPathDB; HostDB:ENSG00000155368; -.
DR eggNOG; KOG0817; Eukaryota.
DR GeneTree; ENSGT00940000154846; -.
DR HOGENOM; CLU_118853_4_1_1; -.
DR InParanoid; P07108; -.
DR OMA; RYKFEAW; -.
DR OrthoDB; 1588000at2759; -.
DR PhylomeDB; P07108; -.
DR TreeFam; TF335802; -.
DR PathwayCommons; P07108; -.
DR Reactome; R-HSA-77289; Mitochondrial Fatty Acid Beta-Oxidation.
DR SignaLink; P07108; -.
DR SIGNOR; P07108; -.
DR BioGRID-ORCS; 1622; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; DBI; human.
DR EvolutionaryTrace; P07108; -.
DR GeneWiki; Diazepam_binding_inhibitor; -.
DR GenomeRNAi; 1622; -.
DR Pharos; P07108; Tbio.
DR PRO; PR:P07108; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P07108; protein.
DR Bgee; ENSG00000155368; Expressed in mammalian vulva and 210 other tissues.
DR ExpressionAtlas; P07108; baseline and differential.
DR Genevisible; P07108; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0032994; C:protein-lipid complex; IDA:UniProtKB.
DR GO; GO:0030156; F:benzodiazepine receptor binding; TAS:ProtInc.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0036042; F:long-chain fatty acyl-CoA binding; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IBA:GO_Central.
DR GO; GO:1903060; P:negative regulation of protein lipidation; IDA:UniProtKB.
DR GO; GO:0036151; P:phosphatidylcholine acyl-chain remodeling; IDA:UniProtKB.
DR GO; GO:1905920; P:positive regulation of CoA-transferase activity; IDA:UniProtKB.
DR GO; GO:2001140; P:positive regulation of phospholipid transport; IDA:UniProtKB.
DR CDD; cd00435; ACBP; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR InterPro; IPR022408; Acyl-CoA-binding_prot_CS.
DR InterPro; IPR000582; Acyl-CoA-binding_protein.
DR InterPro; IPR035984; Acyl-CoA-binding_sf.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR Pfam; PF00887; ACBP; 1.
DR PRINTS; PR00689; ACOABINDINGP.
DR SUPFAM; SSF47027; SSF47027; 1.
DR PROSITE; PS00880; ACB_1; 1.
DR PROSITE; PS51228; ACB_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative promoter usage;
KW Alternative splicing; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Hydroxylation; Lipid-binding; Phosphoprotein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3525533,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT CHAIN 2..87
FT /note="Acyl-CoA-binding protein"
FT /id="PRO_0000214004"
FT DOMAIN 2..87
FT /note="ACB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00573"
FT BINDING 14
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:17044054,
FT ECO:0007744|PDB:2CB8"
FT BINDING 29..33
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:17044054,
FT ECO:0007744|PDB:2CB8"
FT BINDING 55
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:17044054,
FT ECO:0007744|PDB:2CB8"
FT BINDING 74
FT /ligand="an acyl-CoA"
FT /ligand_id="ChEBI:CHEBI:58342"
FT /evidence="ECO:0000269|PubMed:17044054,
FT ECO:0007744|PDB:2CB8"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:3525533,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 8
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 17
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 29
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 55
FT /note="N6-(2-hydroxyisobutyryl)lysine; alternate"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 55
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT MOD_RES 77
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 77
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P31786"
FT VAR_SEQ 1..3
FT /note="MSQ -> MWGDLWLLPPASANPGTGTE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:20345851, ECO:0000303|PubMed:3020548"
FT /id="VSP_000068"
FT VAR_SEQ 1..3
FT /note="MSQ -> MPAF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16055366"
FT /id="VSP_038680"
FT VAR_SEQ 1..3
FT /note="MSQ -> MSQHRAGRRGGVGKRGVRGRELGGQGKYGAGCSECGTRRIAARGE
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:20345851"
FT /id="VSP_043437"
FT VAR_SEQ 1..3
FT /note="MSQ -> MERWGKGLHGLEERGDSVPIPKHRAGRRGGVGKRGVRGRELGGQG
FT KYGAGCSECGTRRIAARGE (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:20345851"
FT /id="VSP_043438"
FT VAR_SEQ 43..87
FT /note="ERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKKKYGI -> GMQ
FT SGGWKGICSSKQAQQLRLEVPGNFTLKLPEALLFRWGMVMVPEVEKTMFRILSVSSSNR
FT IQILVLEGLYWPSPAATLY (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:21698759"
FT /id="VSP_044114"
FT VARIANT 39
FT /note="D -> N (in dbSNP:rs8192504)"
FT /id="VAR_048160"
FT VARIANT 71
FT /note="M -> V (in dbSNP:rs8192506)"
FT /id="VAR_048161"
FT VARIANT 86
FT /note="G -> R (in dbSNP:rs8192507)"
FT /id="VAR_048162"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:2CB8"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2CB8"
FT HELIX 22..36
FT /evidence="ECO:0007829|PDB:2CB8"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:2CB8"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:2CB8"
FT HELIX 67..85
FT /evidence="ECO:0007829|PDB:2CB8"
SQ SEQUENCE 87 AA; 10044 MW; B343A309F1B1AE28 CRC64;
MSQAEFEKAA EEVRHLKTKP SDEEMLFIYG HYKQATVGDI NTERPGMLDF TGKAKWDAWN
ELKGTSKEDA MKAYINKVEE LKKKYGI
